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Toxins 2015, 7(1), 34-42; doi:10.3390/toxins7010034

Plectasin, First Animal Toxin-Like Fungal Defensin Blocking Potassium Channels through Recognizing Channel Pore Region

1
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China
2
Center for BioDrug Research, Wuhan University, Wuhan 430072, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Jean-Marc Sabatier
Received: 7 November 2014 / Accepted: 24 December 2014 / Published: 5 January 2015
(This article belongs to the Special Issue Ion Channel Neurotoxins)
View Full-Text   |   Download PDF [756 KB, uploaded 5 January 2015]   |  

Abstract

The potassium channels were recently found to be inhibited by animal toxin-like human β-defensin 2 (hBD2), the first defensin blocker of potassium channels. Whether there are other defensin blockers from different organisms remains an open question. Here, we reported the potassium channel-blocking plectasin, the first defensin blocker from a fungus. Based on the similar cysteine-stabilized alpha-beta (CSαβ) structure between plectasin and scorpion toxins acting on potassium channels, we found that plectasin could dose-dependently block Kv1.3 channel currents through electrophysiological experiments. Besides Kv1.3 channel, plectasin could less inhibit Kv1.1, Kv1.2, IKCa, SKCa3, hERG and KCNQ channels at the concentration of 1 μΜ. Using mutagenesis and channel activation experiments, we found that outer pore region of Kv1.3 channel was the binding site of plectasin, which is similar to the interacting site of Kv1.3 channel recognized by animal toxin blockers. Together, these findings not only highlight the novel function of plectasin as a potassium channel inhibitor, but also imply that defensins from different organisms functionally evolve to be a novel kind of potassium channel inhibitors. View Full-Text
Keywords: plectasin; defensin; potassium channels; Kv1.3 channel; molecular mechanism; functional evolution plectasin; defensin; potassium channels; Kv1.3 channel; molecular mechanism; functional evolution
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Xiang, F.; Xie, Z.; Feng, J.; Yang, W.; Cao, Z.; Li, W.; Chen, Z.; Wu, Y. Plectasin, First Animal Toxin-Like Fungal Defensin Blocking Potassium Channels through Recognizing Channel Pore Region. Toxins 2015, 7, 34-42.

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